(S)-2-hydroxy-acid oxidase

Class of enzymes

(S)-2-hydroxy-acid oxidase

Glycolate oxidase tetramer, Human

Identifiers
EC no.| 1.1.3.15
CAS no.| 9037-63-2
Databases
IntEnz| IntEnz view
BRENDA| BRENDA entry
ExPASy| NiceZyme view
KEGG| KEGG entry
MetaCyc| metabolic pathway
PRIAM| profile
PDB structures| RCSB PDB PDBe PDBsum
Gene Ontology| AmiGO  / QuickGO
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PMC| articles
PubMed| articles
NCBI| proteins

In enzymology, an (S)-2-hydroxy-acid oxidase (EC 1.1.3.15) is an enzyme that catalyzes the chemical reaction

(S)-2-hydroxy acid + O2 ⇌ {\displaystyle \rightleftharpoons } 2-oxo acid + H2O2

Thus, the two substrates of this enzyme are (S)-2-hydroxy acid and O2, whereas its two products are 2-oxo acid and H2O2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is (S)-2-hydroxy-acid:oxygen 2-oxidoreductase. Other names in common use include glycolate oxidase, hydroxy-acid oxidase A, hydroxy-acid oxidase B, oxidase, L-2-hydroxy acid, hydroxyacid oxidase A, L-alpha-hydroxy acid oxidase, and L-2-hydroxy acid oxidase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, FMN.

## Structural studies

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As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1AL7, 1AL8, 1GYL, 1TB3, and 2NZL.

## References

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* Blanchard M, Green DE, Nocito-Carroll V, Ratner S (1946). "l-Hydroxy acid oxidase" (PDF). J. Biol. Chem. 163 (1): 137–144\. doi:10.1016/S0021-9258(17)41353-6. PMID 21023634.
* FRIGERIO NA, HARBURY HA (1958). "Preparation and some properties of crystalline glycolic acid oxidase of spinach". J. Biol. Chem. 231 (1): 135–57\. doi:10.1016/S0021-9258(19)77292-5. PMID 13538955.
* KUN E, DECHARY JM, PITOT HC (1954). "The oxidation of glycolic acid by a liver enzyme". J. Biol. Chem. 210 (1): 269–80\. doi:10.1016/S0021-9258(18)65451-1. PMID 13201588.
* Nakano M, Danowski TS (1966). "Crystalline mammalian L-amino acid oxidase from rat kidney mitochondria". J. Biol. Chem. 241 (9): 2075–83\. doi:10.1016/S0021-9258(18)96668-8. PMID 5946631.
* Nakano M, Ushijima Y, Saga M, Tsutsumi Y, Asami H (1968). "Aliphatic L-alpha-hydroxyacid oxidase from rat livers: purification and properties". Biochim. Biophys. Acta. 167 (1): 9–22\. doi:10.1016/0005-2744(68)90273-8. PMID 5686300.
* Schuman M, Massey V (1971). "Purification and characterization of glycolic acid oxidase from pig liver" (PDF). Biochim. Biophys. Acta. 227 (3): 500–20\. doi:10.1016/0005-2744(71)90003-9. hdl:2027.42/33685. PMID 5569122.
* Phillips DR, Duley JA, Fennell DJ, Holmes RS (1976). "The self-association of L-alpha hydroxyacid oxidase". Biochim. Biophys. Acta. 427 (2): 679–87\. doi:10.1016/0005-2795(76)90211-7. PMID 1268224.
* Rembeza E, Engqvist MK (2021). "Experimental and computational investigation of enzyme functional annotations uncovers misannotation in the EC 1.1.3.15 enzyme class". PLOS Comput Biol. 17 (9): e1009446. Bibcode:2021PLSCB..17E9446R. doi:10.1371/journal.pcbi.1009446. PMC 8491902. PMID 34555022.

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Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor|

* 3-hydroxyacyl-CoA dehydrogenase
* 3-hydroxybutyryl-CoA dehydrogenase
* Alcohol dehydrogenase
* Aldo-keto reductase
* 1A1
* 1B1
* 1B10
* 1C1
* 1C3
* 1C4
* 7A2
* Aldose reductase
* Beta-Ketoacyl ACP reductase
* Carbohydrate dehydrogenases
* Carnitine dehydrogenase
* D-malate dehydrogenase (decarboxylating)
* DXP reductoisomerase
* Glucose-6-phosphate dehydrogenase
* Glycerol-3-phosphate dehydrogenase
* HMG-CoA reductase
* IMP dehydrogenase
* Isocitrate dehydrogenase
* Lactate dehydrogenase
* L-threonine dehydrogenase
* L-xylulose reductase
* Malate dehydrogenase
* Malate dehydrogenase (decarboxylating)
* Malate dehydrogenase (NADP+)
* Malate dehydrogenase (oxaloacetate-decarboxylating)
* Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
* Phosphogluconate dehydrogenase
* Sorbitol dehydrogenase

* Hydroxysteroid dehydrogenase: 3β
* 3β-HSD
* NSDHL
* 11β
* 11β-HSD1
* 11β-HSD2
* 17β

1.1.2: cytochrome acceptor|

* D-lactate dehydrogenase (cytochrome)
* D-lactate dehydrogenase (cytochrome c-553)
* Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor|

* Glucose oxidase
* L-gulonolactone oxidase
* Xanthine oxidase
* Alcohol oxidase

1.1.4: disulfide as acceptor|

* Vitamin K epoxide reductase
* Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor|

* Malate dehydrogenase (quinone)
* Quinoprotein glucose dehydrogenase

1.1.99: other acceptors|

* Choline dehydrogenase
* L2HGDH

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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